Bestatin, an Aminopeptidase Inhibitor, Promotes Follicular Growth and Ovulation Suppressed by Stress in Mice.

Nakamura, Kimihiko; Fujiwara, Hiroshi; Higuchi, Toshihiro; Honda, Tetsuro; Yamada, Shigetoshi; Nakayama, Takahiro; Fujita, Jun; Maeda, Masako; Tachibana, Toshiyuki; Suginami, Hiroshi; Mori, Takahide

doi:10.1507/endocrj.45.547

Cited by 8 publications

(8 citation statements)

References 25 publications

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“…The cell surface peptidases on both cells can modify the peptide concentration around them and regulate follicular function and growth by controlling the biological activity of these peptides. ovarian response to gonadotropins was suppressed by various stresses [33]. These findings suggest that membrane-bound aminopeptidase(s) are involved in folliculogenesis in vivo.…”

Section: Expression O F Aminopeptidase-n (Ap-n) In the Ovarymentioning

confidence: 72%

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Membrane-Bound Cell Surface Peptidases in Reproductive Organs.

et al. 1999

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Section: Expression O F Aminopeptidase-n (Ap-n) In the Ovarymentioning

confidence: 72%

“…In animal experiments, bestatin administration enhanced murine follicular growth and ovulation including the mice whose follicular growth was suppressed by stress [32,33].…”

Section: Expression Of Ece-1 In the Ovarymentioning

confidence: 99%

Membrane-Bound Cell Surface Peptidases in Reproductive Organs.

et al. 1999

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“…When bestatin was systemically or intrabursally administrated to ovulation‐induced female ICR mice, bestatin significantly increased ovulation 56 . In addition, bestatin significantly enhanced follicular growth and ovulation under the conditions in which the ovarian response to gonadotropins was suppressed by various stresses 57 …”

Section: Local Regulation Of Ovarian Functions By Membrane‐bound Cellmentioning

confidence: 99%

“…IN MICE, BESTATIN promoted follicular growth and ovulation even when follicular growth was suppressed by stress 56,57 . Although the precise mechanism(s) of the effect of bestatin remains unknown, the potential for clinical use should be noted, especially in infertile patients who poorly respond to exogenous gonadotropin therapy for follicular growth induction.…”

Section: Clinical Application Of Peptidase Inhibitors For Reproductivmentioning

confidence: 99%

Functional roles of cell surface peptidases in reproductive organs

Fujiwara

2004

Reprod Medicine & Biology

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A number of biologically active peptides have been proposed to regulate function and differentiation of reproductive organs in an autocrine and/or paracrine fashion. Regulation of the local concentrations of these peptides is one of the important factors influencing their physiological effects on target cells. Membrane-bound cell surface peptidases can activate or inactivate biologically active peptides before peptide factors access their receptors on the cell surface. Aminopeptidase A (EC 3.4.11.7), placental leucine aminopeptidase (EC 3.4.11.3), aminopeptidase-N/CD13 (EC 3.4.11.2), dipeptidyl peptidases IV/CD26 (EC.3.4.14.5), carboxypeptidase-M (EC 3.4.17.12), neutral endopeptidase/CD10 (EC 3.4.24.11) and endothelin converting enzyme-1 (EC 3.4.23) are differentially expressed on the ovary, endometrium and placenta. The inhibition of enzyme activity affects steroid hormone production by granulosa and thecal cells, decidualization of endometrium and migration of extravillous trophoblasts. These findings suggest that membrane-bound cell surface peptidases are local regulators for cellular growth and differentiation in reproductive organs by controlling extracellular concentration of peptide factors. (Reprod Med Biol 2004; : 165 -176).

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“…Moreover, AP inhibitors, bestatin and puromycin, are capable of diminishing cellular proliferation and viability in mammals (Takahashi et al 1989, Constam et al 1995. However, bestatin is capable of restoring and promoting follicular growth and ovulation after its suppression by stress (Nakamura et al 1998).…”

Section: Introductionmentioning

confidence: 99%

Peptidase activities in Crotalus durissus terrificus semen

Marinho

Almeida‐Santos²,

Carneiro³

et al. 2008

Reproduction

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To understand the role of peptidases in seminal physiology of Crotalus durissus terrificus, activity levels of representative enzymes in semen and their sensitivities to inhibitors, cofactors, and peptide hormones were evaluated. The existence of seminal fractions and the association of peptidases with these fractions were also characterized for the first time in snakes. The prominent inhibitors of aminopeptidases (APs) were amastatin for acid, basic, and neutral; bestatin for basic; and diprotin A for dipeptidyl-IV. Cystyl and prolylimino APs were similarly susceptible to the majority of these inhibitors. The basic and neutral were characterized as metallo-peptidases, acid AP was activated by MnCl 2 , and cystyl, prolyl-imino, and type I pyroglutamyl were characterized as sulphydryl-dependent APs. Angiotensin II, vasotocin, bradykinin, fertilization-promoting peptide, and TRH altered the majority of these peptidase activities; these peptides are possible substrates and/or modulators of these peptidases. Peptidase activities were found in all seminal fractions: seminal plasma (SP), prostasome-like (PR) structures, and soluble (S-) and membrane-bound fractions (MFs) of spermatozoa. The levels of activity of each peptidase varied among different seminal fractions. In SP, the higher activities were puromycin-insensitive neutral and basic APs. In PR, the higher activity was puromycin-insensitive neutral AP. In spermatozoa, the higher activity in subcellular SF was puromycinsensitive neutral, while in MF both puromycin-sensitive and -insensitive neutral APs were equally higher than the other examined peptidases. Data suggested that these peptidases, mainly basic and neutral, have a high relevance in regulating seminal functions of C. d. terrificus. Reproduction (2008) 136 767-776

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Bestatin, an Aminopeptidase Inhibitor, Promotes Follicular Growth and Ovulation Suppressed by Stress in Mice.

Abstract: Abstract.We

Cited by 8 publications

References 25 publications

Membrane-Bound Cell Surface Peptidases in Reproductive Organs.

Membrane-Bound Cell Surface Peptidases in Reproductive Organs.

Functional roles of cell surface peptidases in reproductive organs

Peptidase activities in Crotalus durissus terrificus semen

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